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Pathog Glob Health. 2012 Mar;106(1):12-9.
Bovine lactoferrin-derived peptides as novel broad-spectrum inhibitors of influenza virus.
Ammendolia MG, Agamennone M, Pietrantoni A, Lannutti F, Siciliano RA, De Giulio B, Amici C, Superti F.
Source
National Institute of Health, Rome, Italy.
Abstract
Bovine lactoferrin (bLf) is a multifunctional glycoprotein that plays an important role in innate immunity against infections, including influenza. Here we have dissected bLf into its C- and N-lobes and show that inhibition of influenza virus hemagglutination and cell infection is entirely attributable to the C-lobe and that all major virus subtypes, including H1N1 and H3N2, are inhibited. By far-western blotting and sequencing studies, we demonstrate that bLf C-lobe strongly binds to the HA(2) region of viral hemagglutinin, precisely the highly conserved region containing the fusion peptide. By molecular docking studies, three C-lobe fragments were identified which inhibited virus hemagglutination and infection at fentomolar concentration range. Besides contributing to explain the broad anti-influenza activity of bLf, our findings lay the foundations for exploiting bLf fragments as source of potential anti-influenza therapeutics.
PMID:
22595270
[PubMed - in process]
Pathog Glob Health. 2012 Mar;106(1):12-9.
Bovine lactoferrin-derived peptides as novel broad-spectrum inhibitors of influenza virus.
Ammendolia MG, Agamennone M, Pietrantoni A, Lannutti F, Siciliano RA, De Giulio B, Amici C, Superti F.
Source
National Institute of Health, Rome, Italy.
Abstract
Bovine lactoferrin (bLf) is a multifunctional glycoprotein that plays an important role in innate immunity against infections, including influenza. Here we have dissected bLf into its C- and N-lobes and show that inhibition of influenza virus hemagglutination and cell infection is entirely attributable to the C-lobe and that all major virus subtypes, including H1N1 and H3N2, are inhibited. By far-western blotting and sequencing studies, we demonstrate that bLf C-lobe strongly binds to the HA(2) region of viral hemagglutinin, precisely the highly conserved region containing the fusion peptide. By molecular docking studies, three C-lobe fragments were identified which inhibited virus hemagglutination and infection at fentomolar concentration range. Besides contributing to explain the broad anti-influenza activity of bLf, our findings lay the foundations for exploiting bLf fragments as source of potential anti-influenza therapeutics.
PMID:
22595270
[PubMed - in process]
Bovine lactoferrin-derived peptides as novel broad-spectrum inhibitors of influenza virus.
Ammendolia MG, Agamennone M, Pietrantoni A, Lannutti F, Siciliano RA, De Giulio B, Amici C, Superti F.
Source
National Institute of Health, Rome, Italy.
Abstract
Bovine lactoferrin (bLf) is a multifunctional glycoprotein that plays an important role in innate immunity against infections, including influenza. Here we have dissected bLf into its C- and N-lobes and show that inhibition of influenza virus hemagglutination and cell infection is entirely attributable to the C-lobe and that all major virus subtypes, including H1N1 and H3N2, are inhibited. By far-western blotting and sequencing studies, we demonstrate that bLf C-lobe strongly binds to the HA(2) region of viral hemagglutinin, precisely the highly conserved region containing the fusion peptide. By molecular docking studies, three C-lobe fragments were identified which inhibited virus hemagglutination and infection at fentomolar concentration range. Besides contributing to explain the broad anti-influenza activity of bLf, our findings lay the foundations for exploiting bLf fragments as source of potential anti-influenza therapeutics.
PMID:
22595270
[PubMed - in process]
Pathog Glob Health. 2012 Mar;106(1):12-9.
Bovine lactoferrin-derived peptides as novel broad-spectrum inhibitors of influenza virus.
Ammendolia MG, Agamennone M, Pietrantoni A, Lannutti F, Siciliano RA, De Giulio B, Amici C, Superti F.
Source
National Institute of Health, Rome, Italy.
Abstract
Bovine lactoferrin (bLf) is a multifunctional glycoprotein that plays an important role in innate immunity against infections, including influenza. Here we have dissected bLf into its C- and N-lobes and show that inhibition of influenza virus hemagglutination and cell infection is entirely attributable to the C-lobe and that all major virus subtypes, including H1N1 and H3N2, are inhibited. By far-western blotting and sequencing studies, we demonstrate that bLf C-lobe strongly binds to the HA(2) region of viral hemagglutinin, precisely the highly conserved region containing the fusion peptide. By molecular docking studies, three C-lobe fragments were identified which inhibited virus hemagglutination and infection at fentomolar concentration range. Besides contributing to explain the broad anti-influenza activity of bLf, our findings lay the foundations for exploiting bLf fragments as source of potential anti-influenza therapeutics.
PMID:
22595270
[PubMed - in process]